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Volumn 5, Issue 7, 2006, Pages 723-728

The PERK/eIF2α/ATF4 module of the UPR in hypoxia resistance and tumor growth

Author keywords

ATF4; eIF2 ; Hypoxia; Integrated stress response; PERK; Protein translation; Tumor microenvironment; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; CASPASE 12; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; ETOPOSIDE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 2ALPHA; INITIATION FACTOR 1; INITIATION FACTOR 2; MEMBRANE PROTEIN; PROTEIN BCL X; TRANSCRIPTION FACTOR NRF2; PERK KINASE; PROTEIN KINASE R;

EID: 33751285479     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.5.7.2967     Document Type: Review
Times cited : (311)

References (68)
  • 1
    • 0032053823 scopus 로고    scopus 로고
    • The unique physiology of solid tumors: Opportunities (and problems) for cancer therapy
    • Brown JM, Giaccia AJ. The unique physiology of solid tumors: Opportunities (and problems) for cancer therapy. Cancer Res 1998; 58:1408-16.
    • (1998) Cancer Res , vol.58 , pp. 1408-1416
    • Brown, J.M.1    Giaccia, A.J.2
  • 2
  • 3
    • 0035925098 scopus 로고    scopus 로고
    • Tumor hypoxia: Definitions and current clinical, biologic, and molecular aspects
    • Hockel M, Vaupel P. Tumor hypoxia: Definitions and current clinical, biologic, and molecular aspects. J Natl Cancer Inst 2001; 93:266-76.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 266-276
    • Hockel, M.1    Vaupel, P.2
  • 4
    • 0036984640 scopus 로고    scopus 로고
    • Role of angiogenesis in tumor growth and metastasis
    • Folkman J. Role of angiogenesis in tumor growth and metastasis. Semin Oncol 2002; 29:15-8.
    • (2002) Semin Oncol , vol.29 , pp. 15-18
    • Folkman, J.1
  • 5
    • 27944473896 scopus 로고    scopus 로고
    • Fluctuations in pO2 in poorly and well-oxygenated spontaneous canine tumors before and during fractionated radiation therapy
    • Brurberg KG, Skogmo HK, Graff BA, Olsen DR, Rofstad EK. Fluctuations in pO2 in poorly and well-oxygenated spontaneous canine tumors before and during fractionated radiation therapy. Radiotherapy and Oncology 2005; 77:220-6.
    • (2005) Radiotherapy and Oncology , vol.77 , pp. 220-226
    • Brurberg, K.G.1    Skogmo, H.K.2    Graff, B.A.3    Olsen, D.R.4    Rofstad, E.K.5
  • 6
    • 33644506104 scopus 로고    scopus 로고
    • Direct demonstration of instabilities in oxygen concentrations within the extravascular compartment of an experimental tumor
    • Lanzen J, Braun RD, Klitzman B, Brizel D, Secomb TW, Dewhirst MW. Direct demonstration of instabilities in oxygen concentrations within the extravascular compartment of an experimental tumor. Cancer Res 2006; 66:2219-23.
    • (2006) Cancer Res , vol.66 , pp. 2219-2223
    • Lanzen, J.1    Braun, R.D.2    Klitzman, B.3    Brizel, D.4    Secomb, T.W.5    Dewhirst, M.W.6
  • 9
    • 2942590732 scopus 로고    scopus 로고
    • Exploiting tumour hypoxia in cancer treatment
    • Brown JM, Wilson WR. Exploiting tumour hypoxia in cancer treatment. Nat Rev Cancer 2004; 4:437-47.
    • (2004) Nat Rev Cancer , vol.4 , pp. 437-447
    • Brown, J.M.1    Wilson, W.R.2
  • 10
    • 0022453226 scopus 로고
    • Influence of growth phase, nutrition and hypoxia on heterogeneity of cellular buoyant densities in in vitro tumor model systems
    • Luk CK, Sutherland RM. Influence of growth phase, nutrition and hypoxia on heterogeneity of cellular buoyant densities in in vitro tumor model systems. Int J Cancer 1986; 37:883-90.
    • (1986) Int J Cancer , vol.37 , pp. 883-890
    • Luk, C.K.1    Sutherland, R.M.2
  • 11
    • 1542405875 scopus 로고    scopus 로고
    • Acute hypoxia enhances spontaneous lymph node metastasis in an orthotopic murine model of human cervical carcinoma
    • Cairns RA, Hill RP. Acute hypoxia enhances spontaneous lymph node metastasis in an orthotopic murine model of human cervical carcinoma. Cancer Res 2004; 64:2054-61.
    • (2004) Cancer Res , vol.64 , pp. 2054-2061
    • Cairns, R.A.1    Hill, R.P.2
  • 15
    • 0033803047 scopus 로고    scopus 로고
    • Surviving ischemia: Adaptive responses mediated by hypoxia-inducible factor 1
    • Semenza GL. Surviving ischemia: Adaptive responses mediated by hypoxia-inducible factor 1. J Clin Invest 2000; 106:809-12.
    • (2000) J Clin Invest , vol.106 , pp. 809-812
    • Semenza, G.L.1
  • 16
    • 0032053169 scopus 로고    scopus 로고
    • Oxygen sensing, hypoxia-inducible factor-1 and the regulation of mammalian gene expression
    • Ratcliffe P, O'Rourke J, Maxwell P, Pugh C. Oxygen sensing, hypoxia-inducible factor-1 and the regulation of mammalian gene expression. J Exp Biol 1998; 201:1153-62.
    • (1998) J Exp Biol , vol.201 , pp. 1153-1162
    • Ratcliffe, P.1    O'Rourke, J.2    Maxwell, P.3    Pugh, C.4
  • 17
    • 0029796904 scopus 로고    scopus 로고
    • Unifying theory of hypoxia tolerance: Molecular/metabolic defense and rescue mechanisms for surviving oxygen lack
    • Hochachka PW, Buck LT, Doll CJ, Land SC. Unifying theory of hypoxia tolerance: Molecular/metabolic defense and rescue mechanisms for surviving oxygen lack. Proc Natl Acad Sci USA 1996; 93:9493-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9493-9498
    • Hochachka, P.W.1    Buck, L.T.2    Doll, C.J.3    Land, S.C.4
  • 18
    • 0029074864 scopus 로고
    • Regulation of protein synthesis in human cells exposed to extreme hypoxia
    • Kraggerud SM, SJ, Pettersen EO. Regulation of protein synthesis in human cells exposed to extreme hypoxia. Anticancer Research 1995; 15:683-6.
    • (1995) Anticancer Research , vol.15 , pp. 683-686
    • Kraggerud, S.M.1    Sandvik, J.A.2    Pettersen, E.O.3
  • 19
    • 0030848043 scopus 로고    scopus 로고
    • Role of protein-phosphorylation events in the anoxia signal-transduction pathway leading to the inhibition of total protein synthesis in isolated hepatocytes
    • Tinton S, TNQ, Buc-Calderon P. Role of protein-phosphorylation events in the anoxia signal-transduction pathway leading to the inhibition of total protein synthesis in isolated hepatocytes. Eur J Biochem 1997; 249:121-6.
    • (1997) Eur J Biochem , vol.249 , pp. 121-126
    • Tinton, S.1    Tran-Nguyen, Q.-N.2    Buc-Calderon, P.3
  • 21
    • 0022450587 scopus 로고
    • Regulation of protein metabolism of human cells during and after acute hypoxia
    • Pettersen EO, Juul NO, Ronning OW. Regulation of protein metabolism of human cells during and after acute hypoxia. Cancer Research 1986; 46:4346-51.
    • (1986) Cancer Research , vol.46 , pp. 4346-4351
    • Pettersen, E.O.1    Juul, N.O.2    Ronning, O.W.3
  • 23
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • Dever TE. Translation initiation: Adept at adapting. Trends Biochem Sci 1999; 24:398-403.
    • (1999) Trends Biochem Sci , vol.24 , pp. 398-403
    • Dever, T.E.1
  • 24
    • 0033005366 scopus 로고    scopus 로고
    • Eukaryotic initiation factor eIF2
    • Kimball SR. Eukaryotic initiation factor eIF2. Int J Biochem Cell Biol 1999; 31:25-9.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 25-29
    • Kimball, S.R.1
  • 25
    • 0036837864 scopus 로고    scopus 로고
    • Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha
    • Koumenis C, Naczki C, Koritzinsky M, Rastani S, Diehl A, Sonenberg N, Koromilas A, Wouters BG. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha. Mol Cell Biol 2002; 22:7405-16.
    • (2002) Mol Cell Biol , vol.22 , pp. 7405-7416
    • Koumenis, C.1    Naczki, C.2    Koritzinsky, M.3    Rastani, S.4    Diehl, A.5    Sonenberg, N.6    Koromilas, A.7    Wouters, B.G.8
  • 27
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress
    • 10.1074/jbc.M301107200
    • Ma Y, Hendershot LM. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress 10.1074/jbc.M301107200. J Biol Chem 2003; 278:34864-73.
    • (2003) J Biol Chem , vol.278 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 29
    • 0033168065 scopus 로고    scopus 로고
    • Use of the glucose starvation-inducible glucose-regulated protein 78 promoter in suicide gene therapy of murine fibrosarcoma
    • Gazit G, Hung G, Chen X, Anderson WF, Lee AS. Use of the glucose starvation-inducible glucose-regulated protein 78 promoter in suicide gene therapy of murine fibrosarcoma. Cancer Res 1999; 59:3100-6.
    • (1999) Cancer Res , vol.59 , pp. 3100-3106
    • Gazit, G.1    Hung, G.2    Chen, X.3    Anderson, W.F.4    Lee, A.S.5
  • 31
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 2000; 5:897-904.
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 32
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y, Vattem KM, Sood R, An J, Liang J, Stramm L, Wek RC. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol Cell Biol 1998; 18:7499-509.
    • (1998) Mol Cell Biol , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 33
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2000; 2:326-32.
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 34
    • 0038446405 scopus 로고    scopus 로고
    • The unfolded protein response
    • Liu CY, Kaufman RJ. The unfolded protein response. J Cell Sci 2003; 116:1861-2.
    • (2003) J Cell Sci , vol.116 , pp. 1861-1862
    • Liu, C.Y.1    Kaufman, R.J.2
  • 36
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/cAMP- responsive-element-binding protein (CREB) interact with the CCAAT/enhancer- binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response
    • Fawcett TW, Martindale JL, Guyton KZ, Hai T, Holbrook NJ. Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response. Biochem J 1999; 339:135-41.
    • (1999) Biochem J , vol.339 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 37
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 2000; 6:1099-108.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 38
    • 0141621215 scopus 로고    scopus 로고
    • Induction of Grp78/BiP by translational block: Activation of the grp78 promoter by atf4 through an upstream atf/cre site independent of the endoplasmic reticulum stress elements
    • Luo S, Baumeister P, Yang S, Abcouwer SF, Lee AS. Induction of Grp78/BiP by translational block: Activation of the grp78 promoter by atf4 through an upstream atf/cre site independent of the endoplasmic reticulum stress elements. J Biol Chem 2003; 278:37375-85.
    • (2003) J Biol Chem , vol.278 , pp. 37375-37385
    • Luo, S.1    Baumeister, P.2    Yang, S.3    Abcouwer, S.F.4    Lee, A.S.5
  • 39
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem KM, Wek RC. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci USA 2004; 101:11269-74.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 41
    • 1442307970 scopus 로고    scopus 로고
    • Anoxic induction of ATF-4 through HIF-1-independent pathways of protein stabilization in human cancer cells
    • Ameri K, Lewis CE, Raida M, Sowter H, Hai T, Harris AL. Anoxic induction of ATF-4 through HIF-1-independent pathways of protein stabilization in human cancer cells. Blood 2004; 103:1876-82.
    • (2004) Blood , vol.103 , pp. 1876-1882
    • Ameri, K.1    Lewis, C.E.2    Raida, M.3    Sowter, H.4    Hai, T.5    Harris, A.L.6
  • 46
    • 0033693855 scopus 로고    scopus 로고
    • IRE1 and efferent signaling from the endoplasmic reticulum
    • Urano F, Bertolotti A, Ron D. IRE1 and efferent signaling from the endoplasmic reticulum. J Cell Sci 2000; 113:3697-702.
    • (2000) J Cell Sci , vol.113 , pp. 3697-3702
    • Urano, F.1    Bertolotti, A.2    Ron, D.3
  • 48
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • Ma Y, Hendershot LM. The role of the unfolded protein response in tumour development: Friend or foe? Nat Rev Cancer 2004; 4:966-77.
    • (2004) Nat Rev Cancer , vol.4 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 49
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 2002; 110:1389-98.
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 50
    • 23844481790 scopus 로고    scopus 로고
    • Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis
    • Obeng EA, Boise LH. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2005; 280:29578-87.
    • (2005) J Biol Chem , vol.280 , pp. 29578-29587
    • Obeng, E.A.1    Boise, L.H.2
  • 51
    • 33645124763 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism
    • Di Sano F, Ferraro E, Tufi R, Achsel T, Piacentini M, Cecconi F. Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism. J Biol Chem 2006; 281:2693-700.
    • (2006) J Biol Chem , vol.281 , pp. 2693-2700
    • Di Sano, F.1    Ferraro, E.2    Tufi, R.3    Achsel, T.4    Piacentini, M.5    Cecconi, F.6
  • 52
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 54
    • 20744433673 scopus 로고    scopus 로고
    • Involvement of GADD153 and cardiac ankyrin repeat protein in hypoxia-induced apoptosis of H9c2 cells
    • Han XJ, Chae JK, Lee MJ, You KR, Lee BH, Kim DG. Involvement of GADD153 and cardiac ankyrin repeat protein in hypoxia-induced apoptosis of H9c2 cells. J Biol Chem 2005; 280:23122-9.
    • (2005) J Biol Chem , vol.280 , pp. 23122-23129
    • Han, X.J.1    Chae, J.K.2    Lee, M.J.3    You, K.R.4    Lee, B.H.5    Kim, D.G.6
  • 55
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ. Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21:1249-59.
    • (2001) Mol Cell Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 57
    • 0642345210 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum Ca2+ dynamics by proapoptotic BCL-2 family members
    • Oakes SA, Opferman JT, Pozzan T, Korsmeyer SJ, Scorrano L. Regulation of endoplasmic reticulum Ca2+ dynamics by proapoptotic BCL-2 family members. Biochem Pharmacol 2003; 66:1335-40.
    • (2003) Biochem Pharmacol , vol.66 , pp. 1335-1340
    • Oakes, S.A.1    Opferman, J.T.2    Pozzan, T.3    Korsmeyer, S.J.4    Scorrano, L.5
  • 60
    • 0028216444 scopus 로고
    • Evidence that BCL-2 represses apoptosis by regulating endoplasmic reticulum-associated Ca2+ fluxes
    • Lam M, Dubyak G, Chen L, Nunez G, Miesfeld R, Distelhorst C. Evidence that BCL-2 represses apoptosis by regulating endoplasmic reticulum-associated Ca2+ fluxes. PNAS 1994; 91:6569-73.
    • (1994) PNAS , vol.91 , pp. 6569-6573
    • Lam, M.1    Dubyak, G.2    Chen, L.3    Nunez, G.4    Miesfeld, R.5    Distelhorst, C.6
  • 61
    • 0034604033 scopus 로고    scopus 로고
    • Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
    • Hacki J, Egger L., Monney L, Conus S, Rosse T, Fellay I, Borner C. Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene 2000; 19:2286-95.
    • (2000) Oncogene , vol.19 , pp. 2286-2295
    • Hacki, J.1    Egger, L.2    Monney, L.3    Conus, S.4    Rosse, T.5    Fellay, I.6    Borner, C.7
  • 63
    • 32944478891 scopus 로고    scopus 로고
    • Functional coupling of p38-induced upregulation of BiP and activation of RNA-dependent protein kinase-like endoplasmic reticulum kinase to drug resistance of dormant carcinoma cells
    • Ranganathan AC, Zhang L, Adam AP, Aguirre-Ghiso JA. Functional coupling of p38-induced upregulation of BiP and activation of RNA-dependent protein kinase-like endoplasmic reticulum kinase to drug resistance of dormant carcinoma cells. Cancer Res 2006; 66:1702-11.
    • (2006) Cancer Res , vol.66 , pp. 1702-1711
    • Ranganathan, A.C.1    Zhang, L.2    Adam, A.P.3    Aguirre-Ghiso, J.A.4
  • 64
  • 65
    • 7644242953 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells
    • Fribley A, Zeng Q, Wang CY. Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells. Mol Cell Biol 2004; 24:9695-704.
    • (2004) Mol Cell Biol , vol.24 , pp. 9695-9704
    • Fribley, A.1    Zeng, Q.2    Wang, C.Y.3
  • 67
    • 27844568955 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is necessary and sufficient for reducing topoisomerase II{alpha} protein levels and decreasing sensitivity to topoisomerase-targeted drugs
    • Gray MD, Mann M, Nitiss JL, Hendershot LM. Activation of the unfolded protein response is necessary and sufficient for reducing topoisomerase II{alpha} protein levels and decreasing sensitivity to topoisomerase-targeted drugs. Mol Pharmacol 2005; 68:1699-707.
    • (2005) Mol Pharmacol , vol.68 , pp. 1699-1707
    • Gray, M.D.1    Mann, M.2    Nitiss, J.L.3    Hendershot, L.M.4
  • 68
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu BP, Weissman JS. The FAD- and O2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Molecular Cell 2002; 10:983-94.
    • (2002) Molecular Cell , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2


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